Active site structure of bacteriorhodopsin and mechanism of action. |
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Authors: | H L Crespi J R Ferraro |
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Institution: | Chemistry Division, Argonne National Laboratory Argonne, Illinois 60439 USA |
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Abstract: | Pressure experiments with freeze-dried bacteriorhodopsin indicate that water is an essential part of the chromophore. This observation is combined with already known information on (a) the pH dependence of proton pumping, (b) the secondary protein-chromophore interaction with lysine-40, and (c) the proton transfer in the initial photochemical step to give a detailed structure of the active site and a mechanism for proton pumping which is consistent with the bacteriorhodopsin polypeptide sequence. |
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Keywords: | To whom reprint requests should be addressed |
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